Analytical Data
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Gene name
EPHA4
- Application
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Alternative Names
EPHA4；HEK8；Ephrin type-A receptor 4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P54764
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Expression Region
570-986aa
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AA Sequence
SRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDAS CIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLS EASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFT VIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSR VLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMS YGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRP KFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDW LQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSV QAMRTQMQQMHGRMVPV
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Molecular Weight
73 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
EPHA4 (Ephrin type-A receptor 4) is a member of the Eph family of receptor tyrosine kinases, which play crucial roles in various physiological and pathological processes, including cell signaling, tissue development, and neuronal connectivity. Research has indicated that EPHA4 is involved in the regulation of cell migration, adhesion, and differentiation, making it a significant player in developmental biology and cellular communication. Dysregulation of EPHA4 has been linked to several diseases, including cancer, where it may contribute to tumor growth and metastasis, as well as neurological disorders, where it can affect synaptic plasticity and cognitive function. The production of recombinant EPHA4 protein has become a valuable tool for studying its structure, function, and interactions. By using techniques such as recombinant DNA technology, researchers can generate EPHA4 in a controlled environment, allowing for detailed investigations into its biological roles and therapeutic potential. Furthermore, understanding the signaling pathways mediated by EPHA4 may uncover novel targets for drug development, particularly in cancer therapy and neuroprotection. This research not only contributes to our foundational knowledge of cell signaling mechanics but also opens avenues for innovative treatments aimed at diseases where EPHA4 is implicated.
